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Protein

Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase

Gene

wecA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the first lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis, and an acceptor for the addition of subsequent sugars to complete the biosynthesis of O-antigen lipopolysaccharide (LPS) in many E.coli O types. The apparent affinity of WecA for the polyisoprenyl phosphate substrates increases with the polyisoprenyl chain length. WecA is unable to utilize dolichyl phosphate (Dol-P).4 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol.UniRule annotation2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation1 Publication
  • Mn2+UniRule annotation1 Publication

Enzyme regulationi

Inhibited by tunicamycin.

Kineticsi

  1. KM=5.6 µM for UDP-GlcNAc1 Publication
  2. KM=0.12 µM for UDP-GlcNAc (in the presence of Mg2+)1 Publication
  3. KM=0.19 µM for UDP-GlcNAc (in the presence of Mn2+)1 Publication
  4. KM=1.7 mM for Mg2+1 Publication
  5. KM=0.3 mM for Mn2+1 Publication
  1. Vmax=57 pmol/min/mg enzyme (in the presence of Mg2+)1 Publication
  2. Vmax=56 pmol/min/mg enzyme (in the presence of Mn2+)1 Publication

Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Pathwayi: enterobacterial common antigen biosynthesis

This protein is involved in the pathway enterobacterial common antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobacterial common antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei90 – 901Important in orienting the substrate2 Publications
Sitei91 – 911Important in orienting the substrate; probably interacts with magnesium or manganese2 Publications
Sitei156 – 1561Could be required for catalysis2 Publications
Sitei159 – 1591Could be required for catalysis2 Publications

GO - Molecular functioni

  • drug binding Source: EcoliWiki
  • identical protein binding Source: EcoCyc
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • phospho-N-acetylmuramoyl-pentapeptide-transferase activity Source: EcoliWiki
  • phosphotransferase activity, for other substituted phosphate groups Source: UniProtKB
  • transferase activity, transferring glycosyl groups Source: UniProtKB-KW
  • UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  • cell wall macromolecule biosynthetic process Source: UniProtKB
  • cell wall organization Source: UniProtKB
  • enterobacterial common antigen biosynthetic process Source: EcoCyc
  • lipopolysaccharide biosynthetic process Source: UniProtKB
  • O antigen biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Manganese

Enzyme and pathway databases

BioCyciEcoCyc:GLCNACPTRANS-MONOMER.
ECOL316407:JW3758-MONOMER.
MetaCyc:GLCNACPTRANS-MONOMER.
BRENDAi2.7.8.33. 2026.
UniPathwayiUPA00281.
UPA00566.

Protein family/group databases

TCDBi9.B.146.1.7. the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferaseUniRule annotationCurated (EC:2.7.8.33UniRule annotation2 Publications)
Alternative name(s):
UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase1 PublicationUniRule annotation
Undecaprenyl-phosphate GlcNAc-1-phosphate transferaseUniRule annotation
Gene namesi
Name:wecA1 PublicationUniRule annotation
Synonyms:rfe1 Publication
Ordered Locus Names:b3784, JW3758
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10840. wecA.

Subcellular locationi

  • Cell inner membrane UniRule annotation3 Publications; Multi-pass membrane protein UniRule annotation

  • Note: Localizes to discrete regions in the plasma membrane.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22PeriplasmicCurated
Transmembranei3 – 2321HelicalSequence analysisAdd
BLAST
Topological domaini24 – 4522CytoplasmicCuratedAdd
BLAST
Transmembranei46 – 6621HelicalSequence analysisAdd
BLAST
Topological domaini67 – 682PeriplasmicCurated
Transmembranei69 – 8921HelicalSequence analysisAdd
BLAST
Topological domaini90 – 10516Cytoplasmic1 PublicationAdd
BLAST
Transmembranei106 – 12621HelicalSequence analysisAdd
BLAST
Topological domaini127 – 1315PeriplasmicCurated
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Topological domaini153 – 1575Cytoplasmic1 Publication
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 1868PeriplasmicCurated
Transmembranei187 – 20721HelicalSequence analysisAdd
BLAST
Topological domaini208 – 2125CytoplasmicCurated
Transmembranei213 – 23321HelicalSequence analysisAdd
BLAST
Topological domaini234 – 2418PeriplasmicCurated
Transmembranei242 – 26221HelicalSequence analysisAdd
BLAST
Topological domaini263 – 29331Cytoplasmic1 PublicationAdd
BLAST
Transmembranei294 – 31421HelicalSequence analysisAdd
BLAST
Topological domaini315 – 3173PeriplasmicCurated
Transmembranei318 – 33821HelicalSequence analysisAdd
BLAST
Topological domaini339 – 36729Cytoplasmic2 PublicationsAdd
BLAST

GO - Cellular componenti

  • Gram-negative-bacterium-type cell wall Source: UniProtKB
  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351D → G: Decrease in activity; both in vivo and in vitro. 1 Publication
Mutagenesisi90 – 912DD → EE or GG: Loss of activity in vivo. Decrease in activity in vitro. No change in binding to tunicamycin. 1 Publication
Mutagenesisi90 – 901D → E or N: Reduces slightly the velocity and shows a small increase of the affinity for the transferase. 1 Publication
Mutagenesisi91 – 911D → N: Reduces slightly the velocity and shows a small increase of the affinity for the transferase. 1 Publication
Mutagenesisi94 – 941D → G: No loss in activity; both in vivo and in vitro. 1 Publication
Mutagenesisi156 – 1561D → E or N: Loss of activity. 2 Publications
Mutagenesisi156 – 1561D → E: Loss of activity; both in vivo and in vitro; when associated with E-159. 2 Publications
Mutagenesisi156 – 1561D → G: Loss of activity; both in vivo and in vitro. No binding to tunicamycin; when associated with G-159. 2 Publications
Mutagenesisi159 – 1591D → E or N: The activity is detectable but drastically reduced. 2 Publications
Mutagenesisi159 – 1591D → E: Loss of activity; both in vivo and in vitro; when associated with E-156. 2 Publications
Mutagenesisi159 – 1591D → G: Loss of activity; both in vivo and in vitro. No binding to tunicamycin; when associated with G-156. 2 Publications
Mutagenesisi265 – 2651R → K: Decrease in activity. Reduces binding to tunicamycin. 1 Publication
Mutagenesisi276 – 2761D → G: No loss of activity; both in vivo and in vitro. 1 Publication
Mutagenesisi279 – 2824HIHH → GGGG: Loss of activity. No binding to tunicamycin. 1 Publication
Mutagenesisi279 – 2791H → S: Loss of activity. No binding to tunicamycin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferasePRO_0000108941Add
BLAST

Proteomic databases

PaxDbiP0AC78.

Interactioni

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263322. 310 interactions.
DIPiDIP-48083N.
IntActiP0AC78. 1 interaction.
STRINGi511145.b3784.

Structurei

3D structure databases

ProteinModelPortaliP0AC78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family. WecA subfamily.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105ESV. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275125.
InParanoidiP0AC78.
KOiK02851.
OMAiLPHNFQP.
OrthoDBiEOG60GRWX.
PhylomeDBiP0AC78.

Family and domain databases

HAMAPiMF_02030. WecA_Gammaproteo.
InterProiIPR012750. ECA_WecA-rel.
IPR000715. Glycosyl_transferase_4.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02380. ECA_wecA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AC78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLLTVSTDL ISIFLFTTLF LFFARKVAKK VGLVDKPNFR KRHQGLIPLV
60 70 80 90 100
GGISVYAGIC FTFGIVDYYI PHASLYLACA GVLVFIGALD DRFDISVKIR
110 120 130 140 150
ATIQAAVGIV MMVFGKLYLS SLGYIFGSWE MVLGPFGYFL TLFAVWAAIN
160 170 180 190 200
AFNMVDGIDG LLGGLSCVSF AAIGMILWFD GQTSLAIWCF AMIAAILPYI
210 220 230 240 250
MLNLGILGRR YKVFMGDAGS TLIGFTVIWI LLETTQGKTH PISPVTALWI
260 270 280 290 300
IAIPLMDMVA IMYRRLRKGM SPFSPDRQHI HHLIMRAGFT SRQAFVLITL
310 320 330 340 350
AAALLASIGV LAEYSHFVPE WVMLVLFLLA FFLYGYCIKR AWKVARFIKR
360
VKRRLRRNRG GSPNLTK
Length:367
Mass (Da):40,957
Last modified:November 8, 2005 - v1
Checksum:i6EB11CC80C6B9CC8
GO

Sequence cautioni

The sequence AAA24526.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAB20842.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81T → I in AAB20842 (PubMed:1722555).Curated
Sequence conflicti73 – 731A → V in AAB20842 (PubMed:1722555).Curated
Sequence conflicti116 – 1161K → N in AAG26342 (PubMed:11024259).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75640 Genomic DNA. Translation: AAB20842.1. Different initiation.
M76129 Genomic DNA. Translation: AAA24526.1. Different initiation.
AF248031 Genomic DNA. Translation: AAG26342.1.
M87049 Genomic DNA. Translation: AAA67584.1.
U00096 Genomic DNA. Translation: AAC76789.1.
AP009048 Genomic DNA. Translation: BAE77514.1.
PIRiC65182.
RefSeqiNP_418231.1. NC_000913.3.
WP_001050960.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76789; AAC76789; b3784.
BAE77514; BAE77514; BAE77514.
GeneIDi948789.
KEGGiecj:JW3758.
eco:b3784.
PATRICi32123061. VBIEscCol129921_3900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75640 Genomic DNA. Translation: AAB20842.1. Different initiation.
M76129 Genomic DNA. Translation: AAA24526.1. Different initiation.
AF248031 Genomic DNA. Translation: AAG26342.1.
M87049 Genomic DNA. Translation: AAA67584.1.
U00096 Genomic DNA. Translation: AAC76789.1.
AP009048 Genomic DNA. Translation: BAE77514.1.
PIRiC65182.
RefSeqiNP_418231.1. NC_000913.3.
WP_001050960.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AC78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263322. 310 interactions.
DIPiDIP-48083N.
IntActiP0AC78. 1 interaction.
STRINGi511145.b3784.

Protein family/group databases

TCDBi9.B.146.1.7. the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family.

Proteomic databases

PaxDbiP0AC78.

Protocols and materials databases

DNASUi948789.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76789; AAC76789; b3784.
BAE77514; BAE77514; BAE77514.
GeneIDi948789.
KEGGiecj:JW3758.
eco:b3784.
PATRICi32123061. VBIEscCol129921_3900.

Organism-specific databases

EchoBASEiEB0833.
EcoGeneiEG10840. wecA.

Phylogenomic databases

eggNOGiENOG4105ESV. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275125.
InParanoidiP0AC78.
KOiK02851.
OMAiLPHNFQP.
OrthoDBiEOG60GRWX.
PhylomeDBiP0AC78.

Enzyme and pathway databases

UniPathwayiUPA00281.
UPA00566.
BioCyciEcoCyc:GLCNACPTRANS-MONOMER.
ECOL316407:JW3758-MONOMER.
MetaCyc:GLCNACPTRANS-MONOMER.
BRENDAi2.7.8.33. 2026.

Miscellaneous databases

PROiP0AC78.

Family and domain databases

HAMAPiMF_02030. WecA_Gammaproteo.
InterProiIPR012750. ECA_WecA-rel.
IPR000715. Glycosyl_transferase_4.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02380. ECA_wecA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the rfe-rff gene cluster of Escherichia coli."
    Ohta M., Ina K., Kusuzaki K., Kido N., Arakawa Y., Kato N.
    Mol. Microbiol. 5:1853-1862(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the Escherichia coli rfe gene involved in the synthesis of enterobacterial common antigen. Molecular cloning of the rfe-rff gene cluster."
    Meier-Dieter U., Barr K., Starman R., Hatch L., Rick P.D.
    J. Biol. Chem. 267:746-753(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN ECA BIOSYNTHESIS, PATHWAY.
    Strain: K12 and O8:K27.
  3. "Conserved cytoplasmic motifs that distinguish sub-groups of the polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase family."
    Anderson M.S., Eveland S.S., Price N.P.J.
    FEMS Microbiol. Lett. 191:169-175(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MB2884.
  4. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli."
    Rush J.S., Rick P.D., Waechter C.J.
    Glycobiology 7:315-322(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
  8. "The N-terminal region of the Escherichia coli WecA (Rfe) protein, containing three predicted transmembrane helices, is required for function but not for membrane insertion."
    Amer A.O., Valvano M.A.
    J. Bacteriol. 182:498-503(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF START CODON.
  9. "Conserved amino acid residues found in a predicted cytosolic domain of the lipopolysaccharide biosynthetic protein WecA are implicated in the recognition of UDP-N-acetylglucosamine."
    Amer A.O., Valvano M.A.
    Microbiology 147:3015-3025(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LPS O-ANTIGEN BIOSYNTHESIS, SUBCELLULAR LOCATION, PATHWAY, MUTAGENESIS OF ARG-265; HIS-279 AND 279-HIS--HIS-282.
  10. "Conserved aspartic acids are essential for the enzymic activity of the WecA protein initiating the biosynthesis of O-specific lipopolysaccharide and enterobacterial common antigen in Escherichia coli."
    Amer A.O., Valvano M.A.
    Microbiology 148:571-582(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-35; 90-ASP-ASP-91; ASP-94; ASP-156; 156-ASP--ASP-159; ASP-159 AND ASP-276.
  11. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  12. "Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide."
    Lehrer J., Vigeant K.A., Tatar L.D., Valvano M.A.
    J. Bacteriol. 189:2618-2628(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASP-90; ASP-91; ASP-156 AND ASP-159.

Entry informationi

Entry nameiWECA_ECOLI
AccessioniPrimary (citable) accession number: P0AC78
Secondary accession number(s): P24235
, P76751, Q2M892, Q9F8C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: February 17, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.